AOS1_SOLLC
ID AOS1_SOLLC Reviewed; 534 AA.
AC K4BV52; Q9M464;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Allene oxide synthase 1, chloroplastic {ECO:0000303|PubMed:12351632};
DE Short=LeAOS1 {ECO:0000303|PubMed:12351632};
DE EC=4.2.1.92 {ECO:0000305};
DE AltName: Full=Cytochrome P450 74A {ECO:0000305};
DE Flags: Precursor;
GN Name=AOS1 {ECO:0000303|PubMed:12351632}; OrderedLocusNames=Solyc04g079730;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000312|Proteomes:UP000004994};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Bonny Best;
RX PubMed=10759530; DOI=10.1104/pp.122.4.1335;
RA Sivasankar S., Sheldrick B., Rothstein S.J.;
RT "Expression of allene oxide synthase determines defense gene activation in
RT tomato.";
RL Plant Physiol. 122:1335-1342(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12351632; DOI=10.1074/jbc.m207234200;
RA Itoh A., Schilmiller A.L., McCaig B.C., Howe G.A.;
RT "Identification of a jasmonate-regulated allene oxide synthase that
RT metabolizes 9-hydroperoxides of linoleic and linolenic acids.";
RL J. Biol. Chem. 277:46051-46058(2002).
CC -!- FUNCTION: Cytochrome P450 of the CYP74A subfamily involved in the
CC biosynthesis of jasmonic acid from lipoxygenase-derived hydroperoxides
CC of free fatty acids. Catalyzes the synthesis of unstable allene oxide,
CC which is further converted spontaneously by hydrolysis or cyclization.
CC Can use 13S-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid (13-
CC HPOT) and 13S-hydroperoxy-9(Z),11(E)-octadecadienoic acid (13-HPOD) as
CC substrates. {ECO:0000269|PubMed:10759530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate =
CC (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O;
CC Xref=Rhea:RHEA:25074, ChEBI:CHEBI:15377, ChEBI:CHEBI:36438,
CC ChEBI:CHEBI:58757; EC=4.2.1.92; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers. Detected in stems and roots,
CC but not in leaves and fruits under non-inducing conditions.
CC {ECO:0000269|PubMed:10759530}.
CC -!- INDUCTION: Up-regulated by wounding, elicitors, methyl jasmonate or 12-
CC oxophytodienoic acid (PDA). {ECO:0000269|PubMed:10759530}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AJ271093; CAB88032.1; -; mRNA.
DR RefSeq; NP_001234833.2; NM_001247904.2.
DR AlphaFoldDB; K4BV52; -.
DR SMR; K4BV52; -.
DR STRING; 4081.Solyc04g079730.1.1; -.
DR PaxDb; K4BV52; -.
DR PRIDE; K4BV52; -.
DR EnsemblPlants; Solyc04g079730.1.1; Solyc04g079730.1.1.1; Solyc04g079730.1.
DR GeneID; 606711; -.
DR Gramene; Solyc04g079730.1.1; Solyc04g079730.1.1.1; Solyc04g079730.1.
DR KEGG; sly:606711; -.
DR eggNOG; ENOG502QQNS; Eukaryota.
DR HOGENOM; CLU_045757_0_0_1; -.
DR InParanoid; K4BV52; -.
DR OMA; KVTMAAM; -.
DR OrthoDB; 485250at2759; -.
DR PhylomeDB; K4BV52; -.
DR Proteomes; UP000004994; Chromosome 4.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009978; F:allene oxide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Metal-binding;
KW Oxylipin biosynthesis; Plant defense; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 70..534
FT /note="Allene oxide synthase 1, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436190"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 487
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q96242"
FT CONFLICT 78
FT /note="G -> A (in Ref. 1; CAB88032)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="F -> V (in Ref. 1; CAB88032)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="I -> K (in Ref. 1; CAB88032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 59776 MW; A80D5E175C509412 CRC64;
MASTSLSLPS LKLQFPSHTS SSSRKNSSSY RVSIRPIQAS VSEIPPYISS PSQSPSSSSS
PPVKQAKLPA QKVPGDYGLP LVGPWKDRLD YFYNQGKNEF FKSRIQKHQS TVFRTNMPPG
PFISFNPNVV VLLDGKSFPV LFDVSKVEKK DLFTGTFMPS TDLTGGYRVL SYLDPSEPNH
AKLKKLMFYL LSSRRNEVIP EFHNSYSELF ETLENELSTK GKAGLNAAND QAAFNFLARS
LYGINPQDTE LGTDGPKLIG KWVLFQLHPL LILGLPKVLE DLVMHTFRLP PALVKKDYQR
LYNFFYENST SVLDEAEKIG ISREEACHNL LFATCFNSFG GIKIFFPNML KWIGRAGAKL
HSQLAQEIRS VISSNSGKVT MAAMEKMPLM KSVVYESLRI EPPVASQYGR AKHDMVIESH
DASFEIKEGE LLYGYQPFAT KDPKIFDRSE EFVADRFIGE EGEKLLKHVL WSNGSETENA
SINNKQCAGK DFVVLVSRLL LVELFLRYDS FEIEVGASPL GAAITLTSLR RASF
